› 4i85

X-ray diffraction
1.67Å resolution

Crystal structure of transthyretin in complex with CHF5074 at neutral pH

Released:
DOI: 10.2210/pdb4i85/pdb
PDB entry 4i85 coloured by chain, front view.
PDB entry 4i85 coloured by chain, side view.
PDB entry 4i85 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors.
Zanotti G, Cendron L, Folli C, Florio P, Imbimbo BP, Berni R
FEBS Lett 587 2325-31 (2013)
PMID: 23792159

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 13.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02766 (Residues: 21-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

1 bound ligand:
Ligand H50 2 x H50
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 42.26Å b: 84.86Å c: 63.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 citation in other articles

Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites.
Florio et al. (2015)
9 more

2 mentions without citation

Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.
Saldaño et al. (2017)
1 more